| UniProt ID | UKL1_ARATH | |
|---|---|---|
| UniProt AC | Q9FKS0 | |
| Protein Name | Uridine kinase-like protein 1, chloroplastic | |
| Gene Name | UKL1 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 486 | |
| Subcellular Localization | Plastid, chloroplast . Cytoplasm . Aggregates in granular precipitates restricted to the cytoplasm, when expressed in transfected cells. | |
| Protein Description | Involved in the pyrimidine salvage pathway. The uracil phosphoribosyltransferase (UPRT) activity, that catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate, is unsure.. | |
| Protein Sequence | MPEDSSSLDYAMEKASGPHFSGLRFDGLLSSSPPNSSVVSSLRSAVSSSSPSSSDPEAPKQPFIIGVSGGTASGKTTVCDMIIQQLHDHRVVLVNQDSFYRGLTSEELQRVQEYNFDHPDAFDTEQLLHCAETLKSGQPYQVPIYDFKTHQRRSDTFRQVNASDVIILEGILVFHDSRVRNLMNMKIFVDTDADVRLARRIRRDTVERGRDVNSVLEQYAKFVKPAFDDFVLPSKKYADVIIPRGGDNHVAVDLITQHIHTKLGQHDLCKIYPNVYVIQSTFQIRGMHTLIREKDISKHDFVFYSDRLIRLVVEHGLGHLPFTEKQVVTPTGAVYTGVDFCKKLCGVSIIRSGESMENALRACCKGIKIGKILIHRDGDNGKQLIYEKLPHDISERHVLLLDPVLATGNSANQAIELLIQKGVPEAHIIFLNLISAPEGIHCVCKRFPALKIVTSEIDQCLNQEFRVIPGLGEFGDRYFGTDEEDQ | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 30 | Phosphorylation | LRFDGLLSSSPPNSS CCCCCCCCCCCCCCH | 33.54 | 23776212 | |
| 31 | Phosphorylation | RFDGLLSSSPPNSSV CCCCCCCCCCCCCHH | 47.00 | 23776212 | |
| 32 | Phosphorylation | FDGLLSSSPPNSSVV CCCCCCCCCCCCHHH | 40.79 | 23776212 | |
| 36 | Phosphorylation | LSSSPPNSSVVSSLR CCCCCCCCHHHHHHH | 30.22 | 23776212 | |
| 37 | Phosphorylation | SSSPPNSSVVSSLRS CCCCCCCHHHHHHHH | 32.93 | 23776212 | |
| 40 | Phosphorylation | PPNSSVVSSLRSAVS CCCCHHHHHHHHHHH | 22.84 | 23776212 | |
| 41 | Phosphorylation | PNSSVVSSLRSAVSS CCCHHHHHHHHHHHC | 19.05 | 23776212 | |
| 44 | Phosphorylation | SVVSSLRSAVSSSSP HHHHHHHHHHHCCCC | 38.01 | 23776212 | |
| 47 | Phosphorylation | SSLRSAVSSSSPSSS HHHHHHHHCCCCCCC | 24.99 | 23776212 | |
| 48 | Phosphorylation | SLRSAVSSSSPSSSD HHHHHHHCCCCCCCC | 28.39 | 23776212 | |
| 49 | Phosphorylation | LRSAVSSSSPSSSDP HHHHHHCCCCCCCCC | 38.47 | 23776212 | |
| 50 | Phosphorylation | RSAVSSSSPSSSDPE HHHHHCCCCCCCCCC | 30.65 | 30291188 | |
| 52 | Phosphorylation | AVSSSSPSSSDPEAP HHHCCCCCCCCCCCC | 44.41 | 23776212 | |
| 53 | Phosphorylation | VSSSSPSSSDPEAPK HHCCCCCCCCCCCCC | 41.99 | 23776212 | |
| 54 | Phosphorylation | SSSSPSSSDPEAPKQ HCCCCCCCCCCCCCC | 62.62 | 23776212 | |
| 481 | Phosphorylation | FGDRYFGTDEEDQ-- CCCCCCCCCCCCC-- | 30.27 | 29654922 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of UKL1_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of UKL1_ARATH !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of UKL1_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of UKL1_ARATH !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks."; Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.; Plant Physiol. 150:889-903(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASSSPECTROMETRY. | |